Self-assembly and mineralization of peptide-amphiphile nanofibers

Science. 2001 Nov 23;294(5547):1684-8. doi: 10.1126/science.1063187.

Abstract

We have used the pH-induced self-assembly of a peptide-amphiphile to make a nanostructured fibrous scaffold reminiscent of extracellular matrix. The design of this peptide-amphiphile allows the nanofibers to be reversibly cross-linked to enhance or decrease their structural integrity. After cross-linking, the fibers are able to direct mineralization of hydroxyapatite to form a composite material in which the crystallographic c axes of hydroxyapatite are aligned with the long axes of the fibers. This alignment is the same as that observed between collagen fibrils and hydroxyapatite crystals in bone.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bioartificial Organs
  • Biopolymers / chemistry
  • Biopolymers / metabolism
  • Bone and Bones / chemistry
  • Bone and Bones / metabolism
  • Bone and Bones / ultrastructure*
  • Calcification, Physiologic*
  • Calcium / metabolism
  • Collagen / metabolism
  • Collagen / ultrastructure
  • Crystallization
  • Cysteine / chemistry
  • Cysteine / metabolism
  • Disulfides / chemistry
  • Disulfides / metabolism
  • Dithiothreitol / metabolism
  • Durapatite / chemistry
  • Durapatite / metabolism
  • Extracellular Matrix / chemistry
  • Extracellular Matrix / metabolism
  • Extracellular Matrix / ultrastructure
  • Hydrogen-Ion Concentration
  • Micelles
  • Microscopy, Electron
  • Models, Molecular
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Phosphates / metabolism
  • Phosphoserine / chemistry
  • Phosphoserine / metabolism
  • Protein Structure, Quaternary
  • Regeneration
  • Tissue Engineering / methods*

Substances

  • Biopolymers
  • Disulfides
  • Micelles
  • Peptides
  • Phosphates
  • Phosphoserine
  • Collagen
  • Durapatite
  • Cysteine
  • Calcium
  • Dithiothreitol